Evidence map›Paper›PMID 22544567›Full record

ArticleProtein science : a publication of the Protein Society2012

Protein hydrogen exchange: testing current models.

John J Skinner, Woon K Lim, Sabrina Bédard, Ben E Black, S Walter Englander

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

74 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Mapping HDX-MS Data to Protein Conformations through Training Ensemble-Based Models.Journal of the American Society for Mass Spectrometry · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. ATR-FTIR Biosensors for Antibody Detection and Analysis.International journal of molecular sciences · 2022
    Article
  17. Review
  18. Article
  19. Article
  20. Review

14 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

John J SkinnerJohnson Research Foundation, Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6059, USA. skinnerj@uchicago.edu
Woon K Lim
Sabrina Bédard
Ben E Black
S Walter Englander

Funding

STRUCTURAL BIOLOGY TRAINING PROGRAMT32GM008275 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI WAND, A. JOSHUA · 1988 to 2018
$6.0M
Centromere Identity and FunctionR01GM082989 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI BLACK, BEN E. · 2008 to 2018
$3.6M
NIGMS NIH HHS GM031847NIGMS NIH HHS GM082989NIGMS NIH HHS T32 GM008275
6 · The paper itself

Abstract

To investigate the determinants of protein hydrogen exchange (HX), HX rates of most of the backbone amide hydrogens of Staphylococcal nuclease were measured by NMR methods. A modified analysis was used to improve accuracy for the faster hydrogens. HX rates of both near surface and well buried hydrogens are spread over more than 7 orders of magnitude. These results were compared with previous hypotheses for HX rate determination. Contrary to a common assumption, proximity to the surface of the native protein does not usually produce fast exchange. The slow HX rates for unprotected surface hydrogens are not well explained by local electrostatic field. The ability of buried hydrogens to exchange is not explained by a solvent penetration mechanism. The exchange rates of structurally protected hydrogens are not well predicted by algorithms that depend only on local interactions or only on transient unfolding reactions. These observations identify some of the present difficulties of HX rate prediction and suggest the need for returning to a detailed hydrogen by hydrogen analysis to examine the bases of structure-rate relationships, as described in the companion paper (Skinner et al., Protein Sci 2012;21:996-1005).

Indexed as

Models, ChemicalHydrogenMicrococcal NucleaseNuclear Magnetic Resonance, BiomolecularProtein FoldingStaphylococcusStatic ElectricityHydrogenMicrococcal Nuclease

Identifiers

PMID22544567
PMCPMC3403436

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.